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JMJD8 Functions as a Novel AKT1 Lysine Demethylase

Yujuan Wang1, Yaoyao Zhang1,2, Zehua Li1,2

  • 1High Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.

International Journal of Molecular Sciences
|January 8, 2023
PubMed

Insights

JMJD8 protein acts as a demethylase, modifying AKT1 protein methylation. This regulation impacts AKT1 activity, influencing cell proliferation and development.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • JMJD8 is a member of the JMJD protein family, characterized by its JmjC domain.
  • JMJD8 is implicated in signaling pathways such as AKT/NF-κB, affecting cell proliferation and development.

Purpose of the Study:

  • To investigate the role of JMJD8 as a non-histone demethylase.
  • To explore the demethylation activity of JMJD8 on trimethylated lysine of AKT1.
  • To understand the cellular regulation of AKT1 activity by JMJD8.

Main Methods:

  • In vitro assays using trimethylated AKT1 short peptide and AKT1 protein.
  • In vivo studies to assess JMJD8 demethylation of AKT1.
  • Cellular-level tracking of JMJD8's regulation on AKT1 activity.

Main Results:

  • JMJD8 functions as a mini lysine demethylase.
  • JMJD8 was shown to demethylate trimethylated lysine of AKT1.
  • JMJD8 alters AKT1 protein function by modifying its methylation status.

Conclusions:

  • JMJD8's non-histone demethylase activity is confirmed.
  • JMJD8 directly regulates AKT1 methylation and activity.
  • JMJD8 plays a role in cellular processes through AKT1 modulation.
Keywords:
AKT1JMJD8JmjC domaindemethylasetri-methylated lysine

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